Role of Cobalt in Stabilizing the Molecular Structure of Glucose Isomerase from Streptomyces griseofuscus S-41
スポンサーリンク
概要
- 論文の詳細を見る
The role of cobalt in the stabilization of the molecular structure of glucose isomerase from Streptomyces griseofuscus S-41 was investigated using various denaturants. The enzymatic activity and molar ellipticity at 220nm were significantly reduced in 8M urea solution, but restored to the original values on removing urea. Therefore, the enzyme was thought not to suffer a drastic conformational change with urea. On the other hand, the destruction of ordered structure involving a complete loss of activity was observed from circular dichroism and fluorescence spectra in 6M guanidine hydrochloride solution. The enzyme showed somewhat peculiar behavior in organic solvents; in linear-chained solvents the activity correspondingly decreased with solvent concentrations, whereas it increased slightly in side-chained solvents and acetone. The change in activity observed here were not reflected in the circular dichroism and fluorescence spectra. Three of four cobalt ions originally contained in the enzyme were eliminated by treatment with EDTA or 8M urea without significant loss of activity. However, a cobalt-free enzyme was quite difficult to obtain in stable form. For elimination of all cobalts, drastic treatment was required, such as with 6M guanidine hydrochloride, acid-8M urea or EDTA-8M urea, indicating considerable dissociation into subunits. The cobalt addition showed a protective effect on the enzyme from denaturation in such drastic conditions, whereas it did not in less drastic conditions, with 8M urea or organic solvents. It was, therefore, considered that one of the four cobalts was tightly bound to the enzyme and had an essential role in holding the ordered Conformation, especially the quaternary structure of the enzyme, while the other three were bound loosely and might be less important in stabilizing the structure.
- 社団法人 日本農芸化学会の論文
著者
-
KASUMI Takafumi
National Food Research Institute
-
Tsumura Nobuzo
National Food Research Institute Ministry Of Agriculture Forestry And Fisheries:(present Office)taiy
-
Hayashi Kiyoshi
National Food Research Institute
関連論文
- The Role of Conserved Arginine Residue in Loop 4 of Glycoside Hydrolase Family 10 Xylanases
- Cloning and Expression of Chitin Deacetylase Gene from a Deuteromycete, Colletotrichum lindemuthianum
- PCR Cloning and Expression of the F/10 Family Xylanase Gene from Streptomyces olivaceoviridis E-86
- Substrate Specificity of the α-L-Arabinofuranosidase from Trichoderma reesei
- 647 A putative proline iminopeptidase of Thermotoga maritime with leucine- and lysine-p-nitroanilide hydrolyzing activities
- Syntheses of 4-Methylumbelliferyl-β-D-Xylobioside and 5-Bromo-3-Indolyl-β-D-Xylobioside for Sensitive Detection of Xylanase Activity on Agar Plates
- Purification and Characterization of a Family G/11 β-Xylanase from Streptomyces olivaceoviridis E-86
- Primary Structure Analysis and Functional Expression of Erythrose Reductases from Erythritol-Producing Fungi (Trichosporonoides megachiliensis SNG-42)
- Cloning, Sequencing and Expression of the Cellobiose Phosphorylase Gene of Cellvibrio gilvus
- Characterization of a Thermostable Family 10 Endo-Xylanase (XynB) from Thermotoga maritima That Cleaves p-Nitrophenyl-β-D-Xlyloside
- Reduction of Allergenic Proteins by the Effect of the ripening inhibitor (rin) Mutant Gene in an F_1 Hybrid of the rin Mutant Tomato
- Characterization of Cellobiose Phosphorylase and Cellodextrin Phosphorylase (糖質関連酵素化学シンポジウム)
- Cloning and Nucleotide Sequence of the Inulin Fructotransferase (DFA I-Producing)Gene of Arthrobacter globformis S14-3
- Kinetic Studies on the Hydrolysis of N-Acetylated and N-Deacetylated Derivatives of 4-Methylumbelliferyl Chitobioside by the Family 18 Chitinases ChiA and ChiB from Serratia Marcescens
- Purification and Properties of Inulin Fructotransferase (Depolymerizing) from Arthrobacter globiformis C11-1(Microbiology & Fermentation Industry)
- Debittering of Enzymatic Hydrolysates Using an Aminopeptidase from the Edible Basidiomycete Grifola frondosa
- Purification and Characterization of an Aminopeptidase from the Edible Basidiomycete Grifola frondosa
- Ethylene Biosynthesis Regulation in Tomato Fruit from the F_1 Hybrid of the ripening inhibitor (rin) Mutant
- Importance of Five Amino Acid Residues at C-Tarminal Region for the Folding and Stability of β-Glucosidase of Cellvibrio gilvus
- Cloning and Expression of the N-Acetylmuramidase Gene from Streptomyces rutgersensis H-46
- Bacteriolytic Enzyme Produced by Streptomyces sp. : Control of Microorganisms by Means of Lytic Enzymes (II) For Part I, see ref. 6.
- Taxonomical Studies on a Strain of Streptomyces Producing Glucose Isomerase
- Effects of N-Acetylmuramidase from Streptomyces rutgersensis H-46 as a Food Preservative(Food & Nutrition)
- Cultural Conditions for Lytic Enzyme Production by Streptomyces rutgersensis : Control of Microorganisms by Means of Lytic Enzyme.(IV). For Part III, see ref.11.
- A Single Amino Acid Substitution Enhances the Catalytic Activity of Family 11 Xylanase at Alkaline pH
- Breeding of a Mutant of Aureobasidium sp. with High Erythritol Production
- Catalytic Activity of Tripeptidase from Lactococcus lactis to Which Amino Acid Substitution Was Introduced According to Natural Mutation
- Substrate Specificity of a Tripeptidase as a Metalloenzyme Purified from Lactococcus lactis subsp. lactis biovar. diacetylactis ATCC 13675
- Cloning of Inulin Fructotransferase(DFA III-Producing)Gene from Arthrobacter globiformis C11-1
- Cloning and Nucleotide Sequencing of the Aminopeptidase Gene from Aeromonas caviae T-64
- Mutational Analysis of Fungal Family 11 Xylanases on pH Optimum Determination
- Molecular Cloning and Characterization of D-Xylose Isomerase from A Novel Actinobacteria, Thermobifida fusca MBL 10003
- Characterization of a Bacterial Laminaribiose Phosphorylase
- Subunit Structure of Glucose Isomerase from Streptomyces griseofuscus, S-41
- Role of Cobalt in Stabilizing the Molecular Structure of Glucose Isomerase from Streptomyces griseofuscus S-41
- Physicochemical Characterization of N-Acetylmuramidase from Streptomyces rutgersensis H-46
- Purification and Characterization of the Lytic Enzyme Produced by Streptomyces rutgersensis H-46
- Properties of N-Acetylmuramidase from Streptomyces rutgersensis H-46